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Protein

Metallo-beta-lactamase type 2

Gene
N/A
Organism
Bacillus cereus
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Confers resistance to the different beta-lactams antibiotics (penicillin, cephalosporin and carbapenem) via the hydrolysis of the beta-lactam ring. Benzylpenicillin is a better substrate than cephalosporin C and ampicillin (PubMed:3131315, PubMed:2501295).3 Publications

Catalytic activityi

A beta-lactam + H2O = a substituted beta-amino acid.By similarity

Cofactori

Zn2+By similarityNote: Binds 2 Zn2+ ions per subunit.By similarity

Enzyme regulationi

Inhibited by chelating agents such as EDTA.1 Publication

Temperature dependencei

Thermostable.1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi115Zinc 1; via tele nitrogenBy similarity1
Metal bindingi117Zinc 1; via pros nitrogenBy similarity1
Metal bindingi119Zinc 2By similarity1
Metal bindingi178Zinc 1; via tele nitrogenBy similarity1
Metal bindingi197Zinc 2By similarity1
Binding sitei200SubstrateBy similarity1
Binding sitei209Substrate; via amide nitrogenBy similarity1
Metal bindingi239Zinc 2; via tele nitrogenBy similarity1

GO - Molecular functioni

GO - Biological processi

  • antibiotic catabolic process Source: UniProtKB
  • response to antibiotic Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Biological processi

Antibiotic resistance

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

SABIO-RKP14488.

Names & Taxonomyi

Protein namesi
Recommended name:
Metallo-beta-lactamase type 2Curated (EC:3.5.2.6By similarity)
Alternative name(s):
B2 metallo-beta-lactamaseCurated
Beta-lactamase II1 Publication
CephalosporinaseBy similarity
Metallo-beta-lactamase type II1 Publication
Metallothioprotein beta-lactamase II1 Publication
PenicillinaseBy similarity
Zinc-requiring beta-lactamase II1 Publication
OrganismiBacillus cereus
Taxonomic identifieri1396 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillusBacillus cereus group

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Periplasm

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi57H → Y: Inactivates the enzyme. 1 Publication1
Mutagenesisi66E → Q: No change in activity. 1 Publication1
Mutagenesisi110D → N: No change in activity. 1 Publication1
Mutagenesisi117H → Y: Inactivates the enzyme. 1 Publication1
Mutagenesisi119D → N or E: Inactivates the enzyme. 1 Publication1
Mutagenesisi177G → E: Inactivates the enzyme. 1 Publication1
Mutagenesisi241E → Q: No change in activity. 1 Publication1

Chemistry databases

ChEMBLiCHEMBL1744488.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 29Sequence analysis1 PublicationAdd BLAST29
ChainiPRO_000001694330 – 256Metallo-beta-lactamase type 2Add BLAST227

Interactioni

Subunit structurei

Monomer.By similarity

Chemistry databases

BindingDBiP14488.

Structurei

3D structure databases

ProteinModelPortaliP14488.
SMRiP14488.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Signal

Family and domain databases

Gene3Di3.60.15.10. 1 hit.
InterProiIPR001018. Beta-lactamase_class-B_CS.
IPR001279. Metallo-B-lactamas.
[Graphical view]
PfamiPF00753. Lactamase_B. 1 hit.
[Graphical view]
SMARTiSM00849. Lactamase_B. 1 hit.
[Graphical view]
SUPFAMiSSF56281. SSF56281. 1 hit.
PROSITEiPS00743. BETA_LACTAMASE_B_1. 1 hit.
PS00744. BETA_LACTAMASE_B_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P14488-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKNTLLKLGV CVSLLGITPF VSTISSVQAE RTVEHKVIKN ETGTISISQL
60 70 80 90 100
NKNVWVHTEL GYFSGEAVPS NGLVLNTSKG LVLVDSSWDD KLTKELIEMV
110 120 130 140 150
EKKFKKRVTD VIITHAHADR IGGMKTLKER GIKAHSTALT AELAKKNGYE
160 170 180 190 200
EPLGDLQSVT NLKFGNMKVE TFYPGKGHTE DNIVVWLPQY QILAGGCLVK
210 220 230 240 250
SASSKDLGNV ADAYVNEWST SIENVLKRYG NINLVVPGHG EVGDRGLLLH

TLDLLK
Length:256
Mass (Da):28,038
Last modified:January 1, 1990 - v1
Checksum:i670F62378C355C2D
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M19530 Genomic DNA. Translation: AAA22562.1.
PIRiA32017.
RefSeqiWP_000799232.1. NZ_LRRN01000071.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M19530 Genomic DNA. Translation: AAA22562.1.
PIRiA32017.
RefSeqiWP_000799232.1. NZ_LRRN01000071.1.

3D structure databases

ProteinModelPortaliP14488.
SMRiP14488.
ModBaseiSearch...
MobiDBiSearch...

Chemistry databases

BindingDBiP14488.
ChEMBLiCHEMBL1744488.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

SABIO-RKP14488.

Family and domain databases

Gene3Di3.60.15.10. 1 hit.
InterProiIPR001018. Beta-lactamase_class-B_CS.
IPR001279. Metallo-B-lactamas.
[Graphical view]
PfamiPF00753. Lactamase_B. 1 hit.
[Graphical view]
SMARTiSM00849. Lactamase_B. 1 hit.
[Graphical view]
SUPFAMiSSF56281. SSF56281. 1 hit.
PROSITEiPS00743. BETA_LACTAMASE_B_1. 1 hit.
PS00744. BETA_LACTAMASE_B_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiBLAB_BACCE
AccessioniPrimary (citable) accession number: P14488
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 1, 1990
Last sequence update: January 1, 1990
Last modified: November 2, 2016
This is version 85 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Documents

  1. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.